negative regulation of protein glutathionylation

Known as: negative regulation of protein amino acid glutathionylation 
Any process that decreases the rate, frequency, or extent of protein glutathionylation. Protein glutathionylation is the protein modification process… (More)
National Institutes of Health

Papers overview

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2011
2011
Mutation of the ubiquitous cytosolic enzyme Cu/Zn superoxide dismutase (SOD1) is hypothesized to cause familial amyotrophic… (More)
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2010
2010
Endothelial nitric oxide synthase (eNOS) is critical in the regulation of vascular function, and can generate both nitric oxide… (More)
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2010
2010
Reactive oxygen species generated by activated neutrophils can cause oxidative stress and tissue damage. S100A8 (A8) and S100A9… (More)
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Review
2009
Review
2009
S-Glutathionylation is the specific post-translational modification of protein cysteine residues by the addition of the… (More)
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Highly Cited
2009
Highly Cited
2009
Glutathione S-transferase Pi (GSTpi) is a marker protein in many cancers and high levels are linked to drug resistance, even when… (More)
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Review
2008
Review
2008
Protein S-glutathionylation, the reversible binding of glutathione to protein thiols (PSH), is involved in protein redox… (More)
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Review
2007
Review
2007
The specific posttranslational modification of protein cysteine residues by the addition of the tripeptide glutathione is termed… (More)
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2007
2007
Cysteinyl residues in actin are glutathionylated, ie. form a mixed disulfide with glutathione, even in the absence of exogenous… (More)
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Highly Cited
2006
Highly Cited
2006
The skeletal muscle Ca(2+)-release channel (ryanodine receptor type 1 (RyR1)) is a redox sensor, susceptible to reversible S… (More)
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2006
2006
H(2)O(2) produced by stimulation of the macrophage NADPH oxidase is involved both in bacterial killing and as a second messenger… (More)
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